Abstract
We cloned the yloO gene and purified a His-tagged form of its product, the putative protein phosphatase YloO, which we now designate PrpC. This closely resembles the human protein phosphatase PP2C, a member of the PPM family, in sequence and predicted secondary structure. PrpC has phosphatase activity in vitro against a synthetic substrate, p-nitrophenol phosphate, and endogenous Bacillus subtilis proteins. The prkC and prpC genes are adjacent on the chromosome, and the phosphorylated form of PrkC is a substrate for PrpC. These findings suggest that PrkC and PrpC may function as a couple in vivo.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Bacillus subtilis / enzymology*
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Bacillus subtilis / genetics
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Bacillus subtilis / growth & development
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Bacterial Proteins*
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Cloning, Molecular
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Gene Expression
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Genes, Bacterial
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Humans
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Molecular Sequence Data
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Phosphoprotein Phosphatases / classification
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Phosphoprotein Phosphatases / genetics
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Phosphoprotein Phosphatases / isolation & purification
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Phosphoprotein Phosphatases / metabolism*
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Phosphorylation
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Sequence Analysis, DNA
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Sequence Homology, Amino Acid
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Substrate Specificity
Substances
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Bacterial Proteins
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Phosphoprotein Phosphatases